1O1Y

Crystal structure of a glutamine amidotransferase (tm1158) from thermotoga maritima at 1.70 A resolution

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	SSRL BEAMLINE BL11-1
Synchrotron site	SSRL
Beamline	BL11-1
Temperature [K]	100
Detector technology	CCD
Collection date	2002-10-26
Detector	APS-1
Spacegroup name	P 65 2 2
Unit cell lengths	92.362, 92.362, 135.833
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	79.100 * - 1.700
R-factor	0.14651
Rwork	0.145
R-free	0.17200 *
Structure solution method	MAD
RMSD bond length	0.016
RMSD bond angle	1.520 *
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	SOLVE
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	79.100 *	1.790
High resolution limit [Å]	1.700	1.700
Rmerge	0.087 *	0.643 *
Total number of observations	314408 *
Number of reflections	36314
<I/σ(I)>	16	1.7
Completeness [%]	94.9	72.8
Redundancy	8.2	3.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	7.9 *	293	2.4 M Ammonium Sulfate; 0.1 M Bicine pH 9.0, VAPOR DIFFUSION,SITTING DROP,NANODROP, temperature 293K
1	Vapor diffusion *	7.9 *	293	2.4 M Ammonium Sulfate; 0.1 M Bicine pH 9.0, VAPOR DIFFUSION,SITTING DROP,NANODROP, temperature 293K
1	Vapor diffusion *	7.9 *	293	2.4 M Ammonium Sulfate; 0.1 M Bicine pH 9.0, VAPOR DIFFUSION,SITTING DROP,NANODROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	ammonium sulfate	2.4 (M)
2	1	reservoir	Bicine	0.1 (M)	pH9.0
3	1	drop	Tris	20 (mM)	pH7.9
4	1	drop		150 (mM)
5	1	drop	TCEP	0.25 (mM)